Proteomic Exploration of Membrane Curvature Sensors Using a Series of Spherical Supported Lipid Bilayers
Membrane curvature-sensing (MCS) proteins recognize and regulate the morphologies of biological membranes. As these proteins lack characteristic sequence motifs in their primary structure, they are not instantly recognizable by genomic databases. Overcoming this technological challenge toward the ag...
Saved in:
Published in | Analytical chemistry (Washington) Vol. 92; no. 24; pp. 16197 - 16203 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
15.12.2020
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Membrane curvature-sensing (MCS) proteins recognize and regulate the morphologies of biological membranes. As these proteins lack characteristic sequence motifs in their primary structure, they are not instantly recognizable by genomic databases. Overcoming this technological challenge toward the agile identification of new proteins can promote the elucidation of membrane morphological regulation. Here, for the selective identification of MCS proteins, comparative proteomic analysis was performed using different sizes of the spherical supported lipid bilayer (SSLB), which consists of spherical SiO2 particles covered with a lipid bilayer. Because of the presence of SiO2 core, the curvature of the surrounding membrane is well-controlled and stable even on a micron scale. To prove this concept, known membrane curvature-sensing protein domains, Bin/Amphiphysin/Rvs (BAR) and Epsin N-terminal homology (ENTH), were evaluated by performing a binding assay using SSLBs, and the preferential binding to the highly curved membrane was confirmed. Peripheral membrane proteins obtained from normal human dermal fibroblast (NHDF) and human breast cancer (MDA-MB-231) cells were used in shotgun proteomic analysis, and 786 and 949 proteins were identified from SSLBs as lipid membrane binders, respectively. Statistical quantitative analyses of proteins detected from each SSLB with a different size revealed 118 candidate proteins, including 23 proteins unique to MDA-MB-231 cells, as membrane curvature sensors, including some previously reported curvature sensors. Functional clustering analysis based on the KEGG orthology database revealed that the protein-binding property to specific high or low membrane curvature correlated with their functions. Further investigation of candidate proteins will lead to the identification of new MCS proteins as well as cancer biomarkers. |
---|---|
AbstractList | Membrane curvature-sensing (MCS) proteins recognize and regulate the morphologies of biological membranes. As these proteins lack characteristic sequence motifs in their primary structure, they are not instantly recognizable by genomic databases. Overcoming this technological challenge toward the agile identification of new proteins can promote the elucidation of membrane morphological regulation. Here, for the selective identification of MCS proteins, comparative proteomic analysis was performed using different sizes of the spherical supported lipid bilayer (SSLB), which consists of spherical SiO2 particles covered with a lipid bilayer. Because of the presence of SiO2 core, the curvature of the surrounding membrane is well-controlled and stable even on a micron scale. To prove this concept, known membrane curvature-sensing protein domains, Bin/Amphiphysin/Rvs (BAR) and Epsin N-terminal homology (ENTH), were evaluated by performing a binding assay using SSLBs, and the preferential binding to the highly curved membrane was confirmed. Peripheral membrane proteins obtained from normal human dermal fibroblast (NHDF) and human breast cancer (MDA-MB-231) cells were used in shotgun proteomic analysis, and 786 and 949 proteins were identified from SSLBs as lipid membrane binders, respectively. Statistical quantitative analyses of proteins detected from each SSLB with a different size revealed 118 candidate proteins, including 23 proteins unique to MDA-MB-231 cells, as membrane curvature sensors, including some previously reported curvature sensors. Functional clustering analysis based on the KEGG orthology database revealed that the protein-binding property to specific high or low membrane curvature correlated with their functions. Further investigation of candidate proteins will lead to the identification of new MCS proteins as well as cancer biomarkers. Membrane curvature-sensing (MCS) proteins recognize and regulate the morphologies of biological membranes. As these proteins lack characteristic sequence motifs in their primary structure, they are not instantly recognizable by genomic databases. Overcoming this technological challenge toward the agile identification of new proteins can promote the elucidation of membrane morphological regulation. Here, for the selective identification of MCS proteins, comparative proteomic analysis was performed using different sizes of the spherical supported lipid bilayer (SSLB), which consists of spherical SiO particles covered with a lipid bilayer. Because of the presence of SiO core, the curvature of the surrounding membrane is well-controlled and stable even on a micron scale. To prove this concept, known membrane curvature-sensing protein domains, Bin/Amphiphysin/Rvs (BAR) and Epsin N-terminal homology (ENTH), were evaluated by performing a binding assay using SSLBs, and the preferential binding to the highly curved membrane was confirmed. Peripheral membrane proteins obtained from normal human dermal fibroblast (NHDF) and human breast cancer (MDA-MB-231) cells were used in shotgun proteomic analysis, and 786 and 949 proteins were identified from SSLBs as lipid membrane binders, respectively. Statistical quantitative analyses of proteins detected from each SSLB with a different size revealed 118 candidate proteins, including 23 proteins unique to MDA-MB-231 cells, as membrane curvature sensors, including some previously reported curvature sensors. Functional clustering analysis based on the KEGG orthology database revealed that the protein-binding property to specific high or low membrane curvature correlated with their functions. Further investigation of candidate proteins will lead to the identification of new MCS proteins as well as cancer biomarkers. |
Author | Tanaka, Masayoshi Okochi, Mina Yanai, Kentaro Komikawa, Takumi |
AuthorAffiliation | Department of Chemical Science and Engineering |
AuthorAffiliation_xml | – name: Department of Chemical Science and Engineering |
Author_xml | – sequence: 1 givenname: Masayoshi orcidid: 0000-0002-4701-5352 surname: Tanaka fullname: Tanaka, Masayoshi email: tanaka.m.bn@m.titech.ac.jp – sequence: 2 givenname: Takumi surname: Komikawa fullname: Komikawa, Takumi – sequence: 3 givenname: Kentaro surname: Yanai fullname: Yanai, Kentaro – sequence: 4 givenname: Mina orcidid: 0000-0002-1727-2948 surname: Okochi fullname: Okochi, Mina email: okochi.m.aa@m.titech.ac.jp |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33236623$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kUtP3DAUha2Kqgy0_wAhS92wyXD9iJ0s6Yg-pEFFGlhHjueGMUriYCcI_n0dzcCCRVfXV_rOsX3OCTnqfY-EnDFYMuDs0ti4NL1p7Q67JViQIMpPZMFyDpkqCn5EFgAgMq4BjslJjI8AjAFTX8ixEFwoxcWC7G6DH9F3ztLrl6H1wYzO99Q39Aa7Opge6WoKz2acAtIN9tGHSO-j6x-oSXtwGGd4M-zS2ZqWbqZh8GHELV27wW3pD9eaVwzxK_ncmDbit8M8Jfc_r-9Wv7P1319_VlfrzEjJx8zmRlmJupGcFcqavM61LXNemyY3UFo2vxsbybTAMi9R1UUpt0wqpaXmjRKn5GLvOwT_NGEcq85Fi22bvuKnWHGpJCuKAsqEfv-APvoppEhnSgsuy1zrRMk9ZYOPMWBTDcF1JrxWDKq5iSo1Ub01UR2aSLLzg_lUd7h9F71FnwDYA7P8_eL_ev4D5h6ZXA |
CitedBy_id | crossref_primary_10_1016_j_bbagen_2021_129971 crossref_primary_10_1146_annurev_biophys_011422_100054 crossref_primary_10_1016_j_jbiosc_2021_10_003 crossref_primary_10_1021_acsami_2c18956 crossref_primary_10_1007_s00232_022_00237_x |
Cites_doi | 10.1172/JCI116574 10.1016/j.bpj.2012.12.006 10.1038/nnano.2017.98 10.1002/pmic.200500887 10.1016/j.semcdb.2010.01.010 10.1186/1477-5956-7-5 10.1038/sj.emboj.7601176 10.1038/srep01565 10.1038/emboj.2009.261 10.1002/biot.201800087 10.1016/j.tibs.2017.10.001 10.1126/science.1092586 10.1038/nature02209 10.1002/j.1460-2075.1996.tb00442.x 10.1073/pnas.1423868112 10.1111/j.1365-2958.2010.07117.x 10.1073/pnas.1718285115 10.1074/jbc.M004069200 10.1038/sj.onc.1203080 10.1016/j.cell.2016.07.002 10.1002/gcc.21926 10.1073/pnas.1919116117 10.1242/jcs.114454 10.1038/nchembio.213 10.1016/j.cell.2007.03.040 10.1083/jcb.201604003 10.1074/jbc.M308104200 10.1146/annurev.biophys.37.032807.125912 10.1039/c0cs00056f 10.1021/jacs.9b03927 10.1038/ng0996-69 10.1002/j.1460-2075.1992.tb05317.x 10.1038/31940 10.1002/smll.201102446 10.1083/jcb.201512029 10.1073/pnas.1910166116 10.3816/CLC.2009.n.006 10.1021/acs.chemrev.7b00729 10.1073/pnas.94.16.8569 10.1038/s41467-018-06532-3 10.1016/j.ceb.2016.02.001 10.1021/la9903043 |
ContentType | Journal Article |
Copyright | 2020 American
Chemical Society Copyright American Chemical Society Dec 15, 2020 |
Copyright_xml | – notice: 2020 American Chemical Society – notice: Copyright American Chemical Society Dec 15, 2020 |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QF 7QO 7QQ 7SC 7SE 7SP 7SR 7TA 7TB 7TM 7U5 7U7 7U9 8BQ 8FD C1K F28 FR3 H8D H8G H94 JG9 JQ2 KR7 L7M L~C L~D P64 7X8 |
DOI | 10.1021/acs.analchem.0c04039 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Aluminium Industry Abstracts Biotechnology Research Abstracts Ceramic Abstracts Computer and Information Systems Abstracts Corrosion Abstracts Electronics & Communications Abstracts Engineered Materials Abstracts Materials Business File Mechanical & Transportation Engineering Abstracts Nucleic Acids Abstracts Solid State and Superconductivity Abstracts Toxicology Abstracts Virology and AIDS Abstracts METADEX Technology Research Database Environmental Sciences and Pollution Management ANTE: Abstracts in New Technology & Engineering Engineering Research Database Aerospace Database Copper Technical Reference Library AIDS and Cancer Research Abstracts Materials Research Database ProQuest Computer Science Collection Civil Engineering Abstracts Advanced Technologies Database with Aerospace Computer and Information Systems Abstracts Academic Computer and Information Systems Abstracts Professional Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Materials Research Database Technology Research Database Computer and Information Systems Abstracts – Academic Mechanical & Transportation Engineering Abstracts Nucleic Acids Abstracts ProQuest Computer Science Collection Computer and Information Systems Abstracts Materials Business File Environmental Sciences and Pollution Management Aerospace Database Copper Technical Reference Library Engineered Materials Abstracts Biotechnology Research Abstracts AIDS and Cancer Research Abstracts Advanced Technologies Database with Aerospace ANTE: Abstracts in New Technology & Engineering Civil Engineering Abstracts Aluminium Industry Abstracts Virology and AIDS Abstracts Toxicology Abstracts Electronics & Communications Abstracts Ceramic Abstracts METADEX Biotechnology and BioEngineering Abstracts Computer and Information Systems Abstracts Professional Solid State and Superconductivity Abstracts Engineering Research Database Corrosion Abstracts MEDLINE - Academic |
DatabaseTitleList | Materials Research Database MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Chemistry |
EISSN | 1520-6882 |
EndPage | 16203 |
ExternalDocumentID | 10_1021_acs_analchem_0c04039 33236623 c631836897 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | - .K2 02 1AW 23M 55A 5GY 5RE 5VS 7~N 85S AABXI ABFLS ABMVS ABOCM ABPPZ ABPTK ABUCX ABUFD ACGFS ACGOD ACIWK ACJ ACNCT ACPRK ACS AEESW AENEX AFEFF AFRAH ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH BKOMP CS3 D0L DZ EBS ED ED~ F20 F5P GNL IH9 IHE JG JG~ K2 P2P PQEST PQQKQ ROL RXW TAE TN5 UHB UI2 UKR VF5 VG9 VQA W1F WH7 X X6Y XFK YZZ --- -DZ -~X .DC 4.4 53G 6J9 AAHBH ABHFT ABHMW ABJNI ABQRX ACBEA ACGFO ACKOT ADHLV AGXLV AHGAQ CGR CUPRZ CUY CVF ECM EIF GGK KZ1 LMP NPM XSW ZCA ~02 AAYXX CITATION 7QF 7QO 7QQ 7SC 7SE 7SP 7SR 7TA 7TB 7TM 7U5 7U7 7U9 8BQ 8FD C1K F28 FR3 H8D H8G H94 JG9 JQ2 KR7 L7M L~C L~D P64 7X8 |
ID | FETCH-LOGICAL-a442t-c5a6c4e7f42186ca5b57c952baf5a09c13662ef4173e959e6b894d14667472f63 |
IEDL.DBID | ACS |
ISSN | 0003-2700 |
IngestDate | Fri Aug 16 04:52:04 EDT 2024 Thu Oct 10 18:03:22 EDT 2024 Fri Dec 06 01:53:40 EST 2024 Sat Sep 28 08:30:07 EDT 2024 Thu Dec 17 03:36:47 EST 2020 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 24 |
Language | English |
License | https://doi.org/10.15223/policy-029 https://doi.org/10.15223/policy-037 https://doi.org/10.15223/policy-045 |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-a442t-c5a6c4e7f42186ca5b57c952baf5a09c13662ef4173e959e6b894d14667472f63 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ORCID | 0000-0002-1727-2948 0000-0002-4701-5352 |
PMID | 33236623 |
PQID | 2473249577 |
PQPubID | 45400 |
PageCount | 7 |
ParticipantIDs | proquest_miscellaneous_2464188809 proquest_journals_2473249577 crossref_primary_10_1021_acs_analchem_0c04039 pubmed_primary_33236623 acs_journals_10_1021_acs_analchem_0c04039 |
ProviderPackageCode | JG~ 55A AABXI GNL VF5 7~N ACJ VG9 W1F ACS AEESW AFEFF .K2 ABMVS ABUCX IH9 BAANH AQSVZ ED~ UI2 |
PublicationCentury | 2000 |
PublicationDate | 2020-12-15 |
PublicationDateYYYYMMDD | 2020-12-15 |
PublicationDate_xml | – month: 12 year: 2020 text: 2020-12-15 day: 15 |
PublicationDecade | 2020 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: Washington |
PublicationTitle | Analytical chemistry (Washington) |
PublicationTitleAlternate | Anal. Chem |
PublicationYear | 2020 |
Publisher | American Chemical Society |
Publisher_xml | – name: American Chemical Society |
References | ref9/cit9 ref6/cit6 ref36/cit36 ref3/cit3 ref27/cit27 ref18/cit18 ref11/cit11 ref25/cit25 ref16/cit16 ref29/cit29 ref32/cit32 ref23/cit23 ref39/cit39 ref14/cit14 ref8/cit8 ref5/cit5 ref31/cit31 ref2/cit2 ref34/cit34 ref37/cit37 ref28/cit28 ref40/cit40 ref20/cit20 ref17/cit17 ref10/cit10 ref26/cit26 ref35/cit35 ref19/cit19 ref21/cit21 ref12/cit12 ref15/cit15 ref42/cit42 ref41/cit41 ref22/cit22 ref13/cit13 ref33/cit33 ref4/cit4 ref30/cit30 ref1/cit1 ref24/cit24 ref38/cit38 ref7/cit7 |
References_xml | – ident: ref11/cit11 doi: 10.1172/JCI116574 – ident: ref5/cit5 doi: 10.1016/j.bpj.2012.12.006 – ident: ref34/cit34 doi: 10.1038/nnano.2017.98 – ident: ref27/cit27 doi: 10.1002/pmic.200500887 – ident: ref4/cit4 doi: 10.1016/j.semcdb.2010.01.010 – ident: ref26/cit26 doi: 10.1186/1477-5956-7-5 – ident: ref42/cit42 doi: 10.1038/sj.emboj.7601176 – ident: ref29/cit29 doi: 10.1038/srep01565 – ident: ref31/cit31 doi: 10.1038/emboj.2009.261 – ident: ref23/cit23 doi: 10.1002/biot.201800087 – ident: ref28/cit28 doi: 10.1016/j.tibs.2017.10.001 – ident: ref6/cit6 doi: 10.1126/science.1092586 – ident: ref20/cit20 doi: 10.1038/nature02209 – ident: ref12/cit12 doi: 10.1002/j.1460-2075.1996.tb00442.x – ident: ref32/cit32 doi: 10.1073/pnas.1423868112 – ident: ref24/cit24 doi: 10.1111/j.1365-2958.2010.07117.x – ident: ref36/cit36 doi: 10.1073/pnas.1718285115 – ident: ref9/cit9 doi: 10.1074/jbc.M004069200 – ident: ref15/cit15 doi: 10.1038/sj.onc.1203080 – ident: ref40/cit40 doi: 10.1016/j.cell.2016.07.002 – ident: ref37/cit37 doi: 10.1002/gcc.21926 – ident: ref41/cit41 doi: 10.1073/pnas.1919116117 – ident: ref1/cit1 doi: 10.1242/jcs.114454 – ident: ref30/cit30 doi: 10.1038/nchembio.213 – ident: ref7/cit7 doi: 10.1016/j.cell.2007.03.040 – ident: ref3/cit3 doi: 10.1083/jcb.201604003 – ident: ref13/cit13 doi: 10.1074/jbc.M308104200 – ident: ref2/cit2 doi: 10.1146/annurev.biophys.37.032807.125912 – ident: ref19/cit19 doi: 10.1039/c0cs00056f – ident: ref8/cit8 doi: 10.1021/jacs.9b03927 – ident: ref17/cit17 doi: 10.1038/ng0996-69 – ident: ref10/cit10 doi: 10.1002/j.1460-2075.1992.tb05317.x – ident: ref16/cit16 doi: 10.1038/31940 – ident: ref25/cit25 doi: 10.1002/smll.201102446 – ident: ref33/cit33 doi: 10.1083/jcb.201512029 – ident: ref35/cit35 doi: 10.1073/pnas.1910166116 – ident: ref38/cit38 doi: 10.3816/CLC.2009.n.006 – ident: ref18/cit18 doi: 10.1021/acs.chemrev.7b00729 – ident: ref14/cit14 doi: 10.1073/pnas.94.16.8569 – ident: ref21/cit21 doi: 10.1038/s41467-018-06532-3 – ident: ref39/cit39 doi: 10.1016/j.ceb.2016.02.001 – ident: ref22/cit22 doi: 10.1021/la9903043 |
SSID | ssj0011016 |
Score | 2.4252114 |
Snippet | Membrane curvature-sensing (MCS) proteins recognize and regulate the morphologies of biological membranes. As these proteins lack characteristic sequence... |
SourceID | proquest crossref pubmed acs |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 16197 |
SubjectTerms | Amino acid sequence Binders Binding Biological membranes Biomarkers Breast cancer Cell Line, Tumor Chemistry Cluster analysis Clustering Curvature Fibroblasts - metabolism Homology Humans Lipid bilayers Lipid Bilayers - chemistry Lipid Bilayers - metabolism Lipids Membrane proteins Membrane Proteins - metabolism Membranes Morphology Orthology Proteins Proteomics Sensors Silicon dioxide Silybin - chemistry |
Title | Proteomic Exploration of Membrane Curvature Sensors Using a Series of Spherical Supported Lipid Bilayers |
URI | http://dx.doi.org/10.1021/acs.analchem.0c04039 https://www.ncbi.nlm.nih.gov/pubmed/33236623 https://www.proquest.com/docview/2473249577 https://search.proquest.com/docview/2464188809 |
Volume | 92 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1LT9wwEB4VeoAeoDxKF2hlJC4csqzf-NiuQKgSD2lB4hbZji2qdnfRZnPpr68n2SwvIeCaWHY8M_HM53kB7BtvvKYuZr2oZAIoOmbOaZ2xaDUvpKBOYr7z2bk6vRa_buTNPVB86sFn9ND6smsTUdMeht2eT0LHzQJ8ZDohcDSF-oO51wCRaNshDx2qbarcC7OgQvLlY4X0gpVZa5uTVbhoc3aaIJM_3Wrquv7f8xKOb9zIZ1iZGZ7kRyMpa_AhjNZhqd_2e1uHTw9KE27A7SUWcMCUZdKE6dUcJONIzsIwIexRIP0K73OrSSCDhIXHk5LU8QfEErxyCyUOHmDVApQDgu1DMbC3INguuyA_f_-1aO5vwvXJ8VX_NJt1ZcisEGyaeWmVF0FHge2svJVOam8kczZK2zOecqVYiIJqHow0QbkjI4p0IKuEXFhU_Assjsaj8BWIKpI2LLjltheF1MFarw1FCWGca2E7cJCIls_-qjKvHeaM5viwpWQ-o2QHspaN-V1TqOOV8bstr-8XYEJzbMatdQf25q8TH9CLkig7rnCMEvQoHXtpiq1GRuYLcs5w93z7HR--A8sMMTxlGZW7sDidVOFbMnSm7nst3f8BJgj42w |
link.rule.ids | 314,780,784,2765,27076,27924,27925,56738,56788 |
linkProvider | American Chemical Society |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1LbxMxEB6VcigceBQogQJG4sJh0_hdHyGiCtBUSGlRbyvba4uqbYKy2Ut_fWc22RSQKtSr1_JjZtae8Tw-gA8uumh5yMUgG40Gis1FCNYWInsrK6140JTvPD4yoxP17VSfboDucmFwETWOVLdO_JvqAnyP2jzSFrdy2R9ElD3p7sF9TaiVpBENJ2vnARmkHVAe-VW7jLlbRqF7KdZ_30u3KJvtpXPwGH6ul9vGmpz3m0Xox6t_KjneeT9P4NFKDWWflnLzFDbSdBu2hh362zY8_KNQ4TP49YPKOVACM1sG7bX8ZLPMxukS7e1pYsOGXnebeWITtIxn85q10QjMM3qASzV1nlANA5IKRmCiFOZbMQLPrtjnswtPyv9zODn4cjwcFSuMhsIrJRZF1N5ElWxWBG4VvQ7aRqdF8Fn7gYtcGiNSVtzK5LRLJuw7VeHxbNCOEdnIF7A5nU3TS2Cmwruxkl76QVbaJu-jdZzkRUhple_BRyRaufrH6rJ1nwteUmNHyXJFyR4UHTfL38uyHf_pv9ux_GYCoawkaG5re_B-_Rn5QD4VpOysoT5G8X08BHGInaWorCeUUtDu5as7LPwdbI2Ox4fl4dej76_hgSDrnouC613YXMyb9AZVoEV42wr8NXRYAVc |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LbxMxEB5BkYAeeJRXoICRuHDYEL_rYwlE5dGqUqhUcVnZXlutoEmVzV7665nZ7IaCVCG42pYfM2OPxzOeD-C1iy5aHnIxykajgWJzEYK1hcjeykorHjT9d94_MHtH6tOxPr4E9YWTqLGnunXi064-r3KXYYC_pXKP9MXlnA1HEeVPuutwQ-OBS9Fcu-Pp2oFARmkPlke-1f7X3BW9kG6K9e-66YoLZ6t4Jnfh23rKbbzJ92GzDMN48Uc2x_9a0z24011H2e5Kfu7DtTTbglvjHgVuCzYvJSx8ACeHlNaBPjKzVfBey1c2z2w_naHdPUts3NArb7NIbIoW8nxRszYqgXlGD3GppsZTymVA0sEIVJTCfStGINoVe3f6w5MR8BCOJh--jveKDquh8EqJZRG1N1ElmxWBXEWvg7bRaRF81n7kIpfGiJQVtzI57ZIJO05VeEwbtGdENvIRbMzms_QEmKlQR1bSSz_KStvkfbSOk9wIKa3yA3iDRCu7vVaXrRtd8JIKe0qWHSUHUPQcLc9X6Tv-0n67Z_uvAYSykiC6rR3Aq3U18oF8K0jZeUNtjOI7eBhiF49X4rIeUEpBq5dP_2HiL-Hm4ftJ-eXjwedncFuQkc9FwfU2bCwXTXqON6FleNHK_E_JKwPa |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Proteomic+Exploration+of+Membrane+Curvature+Sensors+Using+a+Series+of+Spherical+Supported+Lipid+Bilayers&rft.jtitle=Analytical+chemistry+%28Washington%29&rft.au=Tanaka%2C+Masayoshi&rft.au=Komikawa%2C+Takumi&rft.au=Yanai%2C+Kentaro&rft.au=Okochi%2C+Mina&rft.date=2020-12-15&rft.issn=0003-2700&rft.eissn=1520-6882&rft.volume=92&rft.issue=24&rft.spage=16197&rft.epage=16203&rft_id=info:doi/10.1021%2Facs.analchem.0c04039&rft.externalDBID=n%2Fa&rft.externalDocID=10_1021_acs_analchem_0c04039 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0003-2700&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0003-2700&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0003-2700&client=summon |